Crystal structure of Acetylornithine aminotransferase (EC 2.6.1.11) (ACOAT) (TM1785) from Thermotoga maritima at 1.40 A resolution

Joint Center for Structural Genomics (JCSG)

Single crystal Si(111) bent (horizontal focusing)

NANODROP, 1.6M Sodium citrate, 0.1M Cacodylate pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

BIOMOLECULE: 1
THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT
SCATTERING SUPPORTS THE ASSIGNMENT OF A DIMER AS A
BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE.

SEQUENCE
THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION
TAG MGSDKIHHHHHH.

1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
2. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.
3. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE
INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY
OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75
FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION.
4. PLP MONOMERS ARE MODELED BASED ON DENSITY AND STRUCTURAL HOMOLOGS.
OCCUPANCIES OF PLP (0.8) ARE ASSIGNED BASED ON DIFFERENCE MAPS.
GOL ARE FROM CRYOPROTECTANT.
5. RAMACHANDRAN OUTLIERS A239 AND B239 ARE SUPPORTED BY DENSITY MAPS.

SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT SCATTERING SUPPORTS THE ASSIGNMENT OF A DIMER AS A BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE.

TM1785, Acetylornithine aminotransferase (EC 2.6.1.11) (ACOAT), Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2, TRANSFERASE